Human glycine N-methyltransferase is unfolded by urea through a compact monomer state

Archives of Biochemistry and Biophysics

Volumn 420, Issue 1, 2003, Pages 153-160

  Luka, Zigmund ^a   Wagner, Conrad ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Conformation; Dissociation; Glycine N methyltransferase; Inactivation; Stability; Unfolding

Indexed keywords

GLOBULAR PROTEIN; GLYCINE; MONOMER; N METHYLTRANSFERASE; RECOMBINANT ENZYME; SOLVENT; TETRAMER; TRYPTOPHAN; UNCLASSIFIED DRUG; UREA;

ARTICLE; CIRCULAR DICHROISM; DISSOCIATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INACTIVATION; FLUORESCENCE SPECTROSCOPY; GEL PERMEATION CHROMATOGRAPHY; HUMAN; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN SECONDARY STRUCTURE;

EID: 0242438047     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.abb.2003.09.009     Document Type: Article

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